Intrinsically unstructured proteins.

TitleIntrinsically unstructured proteins.
Publication TypeJournal Article
Year of Publication2002
AuthorsTompa, P.
JournalTrends Biochem Sci
Volume27
Issue10
Pagination527-33
Date Published2002 Oct
ISSN0968-0004
KeywordsAmino Acid Sequence, Amino Acids, Entropy, Hydrophobic and Hydrophilic Interactions, Models, Molecular, Protein Binding, Protein Conformation, Protein Denaturation, Protein Folding, Proteins, Static Electricity, Structure-Activity Relationship
Abstract

The recent suggestion that the classical structure-function paradigm should be extended to proteins and protein domains whose native and functional state is intrinsically unstructured has received a great deal of support. There is ample evidence that the unstructured state, common to all living organisms, is essential for basic cellular functions; thus it deserves to be recognized as a separate functional and structural category within the protein kingdom. In this review, recent findings are surveyed to illustrate that this novel but rapidly advancing field has reached a point where these proteins can be comprehensively classified on the basis of structure and function.

Alternate JournalTrends Biochem. Sci.
PubMed ID12368089